The NAD(P)H-dependent carbonyl reductases catalyze reduction of a variety of endogenous and xenobiotic carbonyl compounds, including biologically and pharmacologically active substrates (Forrest et al., Chem. Biol. Interact., 129, 21-40 (2000)). There is considerable interest in the use of carbonyl reductases in the pharmaceutical and fine chemicals industries for the production of chiral alcohols, which are important building blocks for the synthesis of chirally-pure compounds, e.g., pharmaceutical agents (Panke et al., Curr. Opin. Biotechnol., 15, 272-279 (2004); Schmid et al., Nature, 409, 258-268 (2001); and Schoemaker et al., Science, 299, 1694-1697 (2003)). For such chiral auxiliaries, production from their corresponding prochiral ketones, the use of carbonyl reductases has advantages over chemo-catalysts in terms of their highly chemo-, enantio-, and regioselectivities. These features make stereospecific carbonyl reductases very useful from both scientific and industrial perspectives (Kroutil et al., Curr. Opin. Chem. Biol., 8, 120-126 (2004)). However, the range of current applications for stereospecific carbonyl reductases remains modest. This can be attributed to several limitations, including the stereospecificity and availability of enzymes. In addition, research on molecular mechanisms of oxidoreductases is still in its infancy. Further, most enzymes that can catalyze asymmetric reductions generally follow Prelog's rule in terms of stereochemical outcomes (Bradshaw et al., J. Org. Chem., 57, 1526-1532 (1992); Ernst et al., Appl. Microbiol. Biotechnol., 66, 629-634 (2005); Niefind et al., J. Mol. Biol., 327, 317-328 (2003); Prelog, Pure Appl. Chem., 9, 119-130 (1964)). Enzymes with anti-Prelog stereospecificity are quite rare, and only few have been isolated and characterized in purified forms (De Wildeman et al., Acc. Chem. Res. 40, 1260-1266, (2007)). Accordingly, stereospecific carbonyl reductases are needed. In particular, stereospecific carbonyl reductases with anti-Prelog stereospecificity are needed.